ID EGFR_HUMAN STANDARD; PRT; 1210 AA. AC P00533; P06268; Q14225; DT 21-JUL-1986 (REL. 01, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE EPIDERMAL GROWTH FACTOR RECEPTOR PRECURSOR (EC 2.7.1.112). GN EGFR OR ERBB1. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 84219729. RA ULLRICH A., COUSSENS L., HAYFLICK J.S., DULL T.J., GRAY A., TAM A.W., RA LEE J., YARDEN Y., LIBERMANN T.A., SCHLESSINGER J., DOWNWARD J., RA MAYES E.L.V., WHITTLE N., WATERFIELD M.D., SEEBURG P.H.; RL NATURE 309:418-425(1984). RN [2] RP SEQUENCE OF 713-924 FROM N.A. RX MEDLINE; 84196372. RA LIN C.R., CHEN W.S., KRUIGER W., STOLARSKY L.S., WEBER W., RA EVANS R.M., VERMA I.M., GILL G.N., ROSENFELD M.G.; RL SCIENCE 224:843-848(1984). RN [3] RP SEQUENCE OF 150-962 FROM N.A. RX MEDLINE; 84245835. RA XU Y., ISHII S., CLARK A.J.L., SULLIVAN M., WILSON R.K., MA D.P., RA ROE B.A., MERLINO G.T., PASTAN I.; RL NATURE 309:806-810(1984). RN [4] RP SEQUENCE OF 1028-1210 FROM N.A. RX MEDLINE; 85046483. RA SIMMEN F.A., GOPE M.L., SCHULZ T.Z., WRIGHT D.A., CARPENTER G., RA O'MALLEY B.W.; RL BIOCHEM. BIOPHYS. RES. COMMUN. 124:125-132(1984). RN [5] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE; 88217333. RA HALEY J., WHITTLE N., BENNETT P., KINCHINGTON D., ULLRICH A., RA WATERFIELD M.; RL ONCOGENE RES. 1:375-396(1987). RN [6] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE; 91107677. RA HALEY J.D., WATERFIELD M.D.; RL J. BIOL. CHEM. 266:1746-1753(1991). RN [7] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE; 85270438. RA ISHII S., XU Y.H., STRATTON R.H., ROE B.A., MERLINO G.T., PASTAN I.; RL PROC. NATL. ACAD. SCI. U.S.A. 82:4920-4924(1985). RN [8] RP SEQUENCE OF 540. RA KOHDA D.; RL SUBMITTED (SEP-1997) TO THE SWISS-PROT DATA BANK. RN [9] RP RECEPTOR ACTIVITY. RX MEDLINE; 84191554. RA MROCZKOWSKI B., MOSIG G., COHEN S.; RL NATURE 309:270-273(1984). RN [10] RP PHOSPHORYLATION. RX MEDLINE; 89278137. RA MARGOLIS B.L., LAX I., KRIS R., DOMBALAGIAN M., HONEGGER A.M., RA HOWK R., GIVOL D., ULLRICH A., SCHLESSINGER J.; RL J. BIOL. CHEM. 264:10667-10671(1989). RN [11] RP REVIEW. RX MEDLINE; 87297456. RA CARPENTER G.; RL ANNU. REV. BIOCHEM. 56:881-914(1987). CC -!- FUNCTION: THE EGF RECEPTOR MEDIATES THE BIOLOGICAL SIGNAL OF EGF CC AND ALSO OF TRANSFORMING GROWTH FACTOR ALPHA AND VACCINIA VIRUS CC GROWTH FACTOR. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- SUBCELLULAR LOCATION: TYPE I MEMBRANE PROTEIN. CC -!- BINDING OF EGF TO THE RECEPTOR LEADS TO INTERNALIZATION OF THE CC EGF-RECEPTOR COMPLEX, INDUCTION OF THE TYROSINE KINASE ACTIVITY, CC STIMULATION OF CELL DNA SYNTHESIS, AND CELL PROLIFERATION. CC -!- SIMILARITY: BELONGS TO THE EGF RECEPTOR FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00588; G757924; -. DR EMBL; X06370; G31119; -. DR EMBL; X00663; E4014; -. DR EMBL; M38425; G553271; -. DR EMBL; M11234; G553272; -. DR PIR; A00641; GQHUE. DR PIR; A00642; GQHUE2. DR PIR; A23062; A23062. DR SWISS-2DPAGE; P00533; HUMAN. DR MIM; 131550; -. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW TRANSMEMBRANE; GLYCOPROTEIN; DUPLICATION; RECEPTOR; SIGNAL; KW TRANSFERASE; TYROSINE-PROTEIN KINASE; ATP-BINDING; PHOSPHORYLATION. FT SIGNAL 1 24 FT CHAIN 25 1210 EGF RECEPTOR. FT DOMAIN 25 645 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 646 668 POTENTIAL. FT DOMAIN 669 1210 CYTOPLASMIC (POTENTIAL). FT REPEAT 75 300 APPROXIMATE. FT REPEAT 390 600 APPROXIMATE. FT DOMAIN 1025 1071 SER-RICH. FT DOMAIN 712 979 PROTEIN KINASE. FT NP_BIND 718 726 ATP (BY SIMILARITY). FT BINDING 745 745 ATP (BY SIMILARITY). FT ACT_SITE 837 837 BY SIMILARITY. FT MOD_RES 678 678 PHOSPHORYLATION (BY PKC). FT MOD_RES 1092 1092 PHOSPHORYLATION (AUTO-). FT MOD_RES 1110 1110 PHOSPHORYLATION (AUTO-). FT MOD_RES 1172 1172 PHOSPHORYLATION (AUTO-). FT MOD_RES 1197 1197 PHOSPHORYLATION (AUTO-, MAJOR SITE). FT CARBOHYD 128 128 POTENTIAL. FT CARBOHYD 175 175 POTENTIAL. FT CARBOHYD 196 196 POTENTIAL. FT CARBOHYD 352 352 POTENTIAL. FT CARBOHYD 361 361 POTENTIAL. FT CARBOHYD 413 413 POTENTIAL. FT CARBOHYD 444 444 POTENTIAL. FT CARBOHYD 528 528 POTENTIAL. FT CARBOHYD 568 568 POTENTIAL. FT CARBOHYD 603 603 POTENTIAL. FT CARBOHYD 623 623 POTENTIAL. FT CONFLICT 540 540 N -> K (IN REF. 1). SQ SEQUENCE 1210 AA; 134277 MW; 19DDD2E4 CRC32; MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV APQSSEFIGA //